ID A0A068VD74_COFCA Unreviewed; 1068 AA.
AC A0A068VD74;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=DH200=94 genomic scaffold, scaffold_285 {ECO:0000313|EMBL:CDP18770.1};
GN ORFNames=GSCOC_T00000120001 {ECO:0000313|EMBL:CDP18770.1};
OS Coffea canephora (Robusta coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=49390 {ECO:0000313|EMBL:CDP18770.1, ECO:0000313|Proteomes:UP000295252};
RN [1] {ECO:0000313|Proteomes:UP000295252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX PubMed=25190796; DOI=10.1126/science.1255274;
RA Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA Lashermes P.;
RT "The coffee genome provides insight into the convergent evolution of
RT caffeine biosynthesis.";
RL Science 345:1181-1184(2014).
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DR EMBL; HG739369; CDP18770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068VD74; -.
DR STRING; 49390.A0A068VD74; -.
DR EnsemblPlants; CDP18770; CDP18770; GSCOC_T00000120001.
DR Gramene; CDP18770; CDP18770; GSCOC_T00000120001.
DR InParanoid; A0A068VD74; -.
DR OMA; KILMSIL; -.
DR PhylomeDB; A0A068VD74; -.
DR Proteomes; UP000295252; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF62; MDIS1-INTERACTING RECEPTOR LIKE KINASE 2-LIKE; 1.
DR Pfam; PF00560; LRR_1; 12.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 13.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000295252};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1068
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001655775"
FT TRANSMEM 731..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 797..1068
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 825
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1068 AA; 117241 MW; CC3A5082D3D0D364 CRC64;
MSSFKMISIF LLVLLFPSFH PKCGASAYAE EALALLKWKA SFQNQNNSFL TSWNLQSIIA
KNSSSLPCTW AGISCVVGGV NRLNLSAWSI KGSLFDFPFS SLPNLEYLDL SHNQIFGCIP
KQIGSLAKLI YLDFSDNNLT GSIPASFCDL NRLVELSLFQ NHLSGPIPSA IGNLTSLQFL
ILNQNNLIGT IPKSLGNLTN LIKLQLNDNQ LSGSIPKELG NLKFLTKMEV GENQLIGSIP
ISIGNLSNLE SLSLQTNQFS GSIPSTFGNL NRLVNLSIYQ NCLSGPIPSE VGNLISLQFL
LLFQNNLTGA IPNSLGNLTN LIQLYLYYNQ FSGSIPKELG DLKCLINIAI SENQLSGSIP
VSIGNLSNLE YFLFQNHLSG PIPSEFGNLI SLQFLFLSQN NLTGAIPKSL GNLTNLIQLY
LYYNQLSGSI PKELGDLKFL TDMGIGENQL NGPIPVAIGN LSSLRRLQLR DNQISGTVPE
ELRNLKKLAF MVLAQNQFSG PLPELLCQNA TLQFIAVSGN MLSGPIPRSL RNCSSLVRAS
GIPPEIGNLT QLRALNLSSN CLSGEIPRAV AKLASMLKLD LHDNQFLGGI PQELGGLVEF
LDLSTNSLSG NLPKLLGDLK HLFHMNLSNN VLSQKIPPQI GNLQSLGMLD LSHNNLSGLI
PKTLAALPGL CRINLSFNNL EGPIPSGRAF ANLTLEEVKG NKGLCGNITG LQACESSPLS
KKHGMDKRKE LVLIIVLPLL GSFMLLGAFF GVLRLHDQRK RNSRAEVMEV KMGNLFAICA
HDAKALYKEI VRSTEEFSEI FCIGKGGYGS VYRAQLPSGD VVAVKRLHNM PNVAKDRNFL
NEIRALTEIK HRNIVKLFGF CSNAQHSILV YEHLERGSLA KILTIEEEAK VLDWQKRLKI
IKGIAHALSY MHHDCSLAIV HRDISSKNIL LDPEYEAHIS DFGTSKFLKK DSSNWSSLAG
TYGYVAPEFA YAMKVDEKCD VYSFGVLTME VIKGKHPGDL IANLMSSNPE DIELKDLLDQ
RLLYPNQEIE KILMSILKLA RECLHADPQC RPTMLLISRS MSACEPSK
//